A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase

Journal of Biological Chemistry

Volumn 290, Issue 6, 2015, Pages 3775-3783

  Kim, In Kwon ^a   Stegeman, Roderick A ^a   Brosey, Chris A ^a   Ellenberger, Tom ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

COMPLEX ASSEMBLY; GLYCOHYDROLASE; HIGH THROUGHPUT SCREENING; LIGAND SPECIFICITY; POLY(ADP RIBOSE) POLYMERASE 1; POST-TRANSLATIONAL MODIFICATIONS; QUANTITATIVE ASSAY; REPAIR PROTEINS;

SCAFFOLDS (BIOLOGY);

GLYCOSIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; POLY(ADENOSINE DIPHOSPHATE RIBOSE)GLYCOHYDROLASE; UNCLASSIFIED DRUG; XRCC1 PROTEIN; ADENOSINE DIPHOSPHATE RIBOSE; DNA BINDING PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PARP1 PROTEIN, HUMAN; POLY ADP-RIBOSE GLYCOHYDROLASE; PROTEIN BINDING; X-RAY REPAIR CROSS COMPLEMENTING PROTEIN 1;

ARTICLE; BINDING AFFINITY; BINDING ASSAY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; FLUORESCENCE RESONANCE ENERGY TRANSFER; LIGAND BINDING; NONHUMAN; PROTEIN DISASSEMBLY; PROTEIN EXPRESSION; PROTEIN METABOLISM; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; QUANTITATIVE ANALYSIS; QUANTITATIVE ASSAY; BINDING SITE; CHEMISTRY; HUMAN; METABOLISM;

ADENOSINE DIPHOSPHATE RIBOSE; BINDING SITES; DNA-BINDING PROTEINS; GLYCOSIDE HYDROLASES; HUMANS; POLY(ADP-RIBOSE) POLYMERASES; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; SUBSTRATE SPECIFICITY;

EID: 84922347288     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.624718     Document Type: Article

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